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Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
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High-affinity cyclic peptide matriptase inhibitors.

Pedro Quimbar1, Uru Malik, Christian P Sommerhoff

  • 1La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria 3086, Australia.

The Journal of Biological Chemistry
|April 4, 2013
PubMed
Summary
This summary is machine-generated.

Cyclic peptides like sunflower trypsin inhibitor-1 and M. cochinchinensis trypsin inhibitor-II were studied for matriptase inhibition. An MCoTI-II analog emerged as a highly potent matriptase inhibitor, offering therapeutic potential.

Keywords:
Molecular ModelingNuclear Magnetic ResonancePeptide ConformationPeptidesProtease Inhibitor

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Area of Science:

  • Biochemistry
  • Medicinal Chemistry
  • Molecular Biology

Background:

  • Sunflower trypsin inhibitor-1 (SFTI-1) and Momordica cochinchinensis trypsin inhibitor-II (MCoTI-II) are cyclic peptides with protease inhibitory activity.
  • Matriptase, a serine protease, is implicated in diseases like cancer due to its role in cell proliferation and extracellular matrix modification.

Purpose of the Study:

  • To analyze the structure-activity relationships of SFTI-1 and MCoTI-II for matriptase inhibition.
  • To design novel, potent, and selective matriptase inhibitors with therapeutic potential.

Main Methods:

  • Positional scanning mutagenesis was employed to generate alanine mutants of SFTI-1 and MCoTI-II.
  • Inhibitory activity against matriptase and trypsin was assessed for wild-type peptides and their mutants.

Main Results:

  • MCoTI-II demonstrated significantly higher matriptase inhibitory activity compared to SFTI-1.
  • While alanine mutations decreased trypsin affinity, several mutations enhanced matriptase inhibitory activity.
  • A designed MCoTI-II analog achieved a 290 pM equilibrium dissociation constant, representing one of the most potent matriptase inhibitors.

Conclusions:

  • Structure-activity relationship analysis provides insights into modulating cyclic peptide affinity for matriptase over trypsin.
  • The findings support the development of selective matriptase inhibitors for therapeutic applications in diseases like cancer.